Self-assembly and gelation properties of α-helix versus β-sheet forming peptides

Saiani, Alberto; Mohammed, Amran; Frielinghaus, Henrich; Collins, Richard F.; Hodson, Nigel; Kielty, Cay M.; Sherratt, Michael J.; Miller, Aline F.

doi:10.1039/b811288f

Cited by 141 publications

(166 citation statements)

References 54 publications

Supporting

Mentioning

154

Contrasting

Order By: Relevance

“…[24][25][26][27][28][29] In the former molecule, the di-glycine spacer was included to promote flexibility between the two octapeptides, and the order of amino acids was specifically designed to include a charge repulsion around the central glycine units to minimize any intra-molecular folding of the extended peptide chain (Figure 1), thus enhancing the ability of FEKII18 to co-assemble into two different fibers of FEKII. Prior to any doping experiments, the characteristic self-assembling behavior of the pure FEKII18 peptide was explored and compared to our previous work on the single FEKII peptide.…”

Section: Resultsmentioning

confidence: 99%

“…24,25 No shoulder was detected in the data for any sample; however, the curves were rather broad suggesting cylinders with multiple diameters were present. This was corroborated as again, no good fits to the data were obtained using a single diameter cylinder.…”

mentioning

confidence: 88%

“…It is well known that FEKII self-assembles in water into anti-parallel b-sheet rich fibers driven by hydrophobic and electrostatic interactions, and these become entangled and form a self-supporting hydrogel when above a critical gelation concentration of 17 mg ml 21 at pH 2 and 5 mg ml 21 at pH 7. [24][25][26][27][28] By adding small quantities of the …”

Section: Introductionmentioning

confidence: 99%

“…This is higher than the 21 value expected for rod-like structures, 35 which was observed for the single peptide. 24 Such a change in the power law behavior from 21 to 21.6 has previously been shown to be due to an increase in the heterogeneity and decrease in the mesh size of the fibrillar network present. 36 This is most likely due to heterogeneity in self-assembly of the Co-Assembling Peptide Hydrogels 671 longer peptide; it essentially contains two self-assembling units, where each is capable of self-assembling with two other units from different molecules, and so on.…”

mentioning

confidence: 95%

See 3 more Smart Citations

Controlling network topology and mechanical properties of co‐assembling peptide hydrogels

2014

View full text Add to dashboard Cite

Oligopeptides are well-known to self-assemble into a wide array of nanostructures including β-sheet-rich fibers that when present above a critical concentration become entangled and form self-supporting hydrogels. The length, quantity, and interactions between fibers influence the mechanical properties of the hydrogel formed and this is typically achieved by varying the peptide concentration, pH, ionic strength, or the addition of a second species or chemical cross-linking agent. Here, we outline an alternative, facile route to control the mechanical properties of the self-assembling octa-peptide, FEFEFKFK (FEKII); simply doping with controlled quantities of its double length peptide, FEFEFKFK-GG-FKFKFEFE (FEKII18). The structure and properties of a series of samples were studied here (0–100 M% of FEKII18) using Fourier transform infrared, small angle X-ray scattering, transmission electron microscopy, and oscillatory rheology. All samples were found to contain elongated, flexible fibers and all mixed samples contained Y-shaped branch points and parallel fibers which is attributed to the longer peptide self-assembling within two fibers, thus creating a cross-link in the network structure. Such behavior was reflected in an increase in the elasticity of the mixed samples with increasing quantity of double peptide. Interestingly the elastic modulus increased up to 30 times the pure FEKII value simply by adding 28 M% of FEKII18. These observations provide an easy, off-the-shelf method for an end-user to control the cross-linked network structure of the peptide hydrogel, and consequently strength of the hydrogel simply by physically mixing pre-determined quantities of two similar peptide molecules.

show abstract

Section: Resultsmentioning

confidence: 99%

mentioning

confidence: 88%

Section: Introductionmentioning

confidence: 99%

mentioning

confidence: 95%

See 2 more Smart Citations

Controlling network topology and mechanical properties of co‐assembling peptide hydrogels

2014

View full text Add to dashboard Cite

show abstract

“…There is a wide variety of natural and synthetic materials currently being employed to create such materials but recent research effort has focused on using natural materials as they are cheap, abundant, and require limited functionalization [5][6][7]. With this in mind we have previously demonstrated that hen egg white lysozyme (HEWL) protein can form hydrogels at physiological pH simply by adding a small quantity of the reductant dithiothreitol (DTT) which encourages the protein to gel under mild conditions [8,9].…”

mentioning

confidence: 99%

Protein Fibrillar Hydrogels for three-Dimensional Tissue Engineering

Yan

Nykänen

Ruokolainen

et al. 2009

Research Letters in Nanotechnology

View full text Add to dashboard Cite

Protein self-assembly into highly ordered fibrillar aggregates has attracted increasing attention over recent years, due primarily to its association with disease states such as Alzheimer's. More recently, however, research has focused on understanding the generic behavior of protein self-assembly where fibrillation is typically induced under harsh conditions of low pH and/or high temperature. Moreover the inherent properties of these fibrils, including their nanoscale dimension, environmental responsiveness, and biological compatibility, are attracting substantial interest for exploiting these fibrils for the creation of new materials. Here we will show how protein fibrils can be formed under physiological conditions and their subsequent gelation driven using the ionic strength of cell culture media while simultaneously incorporating cells homogeneously throughout the gel network. The fibrillar and elastic nature of the gel have been confirmed using cryo-transmission electron microscopy and oscillatory rheology, respectively; while cell culture work shows that our hydrogels promote cell spreading, attachment, and proliferation in three dimensions. Copyright © 2009 Hui Yan et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.Hydrogels have recently attracted increasing attention as tissue engineering scaffolds for repairing and regenerating tissues [1][2][3][4]. There is a wide variety of natural and synthetic materials currently being employed to create such materials but recent research effort has focused on using natural materials as they are cheap, abundant, and require limited functionalization [5][6][7]. With this in mind we have previously demonstrated that hen egg white lysozyme (HEWL) protein can form hydrogels at physiological pH simply by adding a small quantity of the reductant dithiothreitol (DTT) which encourages the protein to gel under mild conditions [8,9]. HEWL was selected as it is a small globular protein and contains both α-helix and β-sheet in its secondary structure and has high solubility in water. We went on to show that the mesh size of the hydrogel and its mechanical properties could be controlled by varying concentration and our two-dimensional cell culture work demonstrated that these hydrogels are cytocompatable [9,10]. However, before these materials can find any tissue engineering application, cells need to be incorporated throughout the hydrogel and their viability explored.In this letter we will outline a novel method for the incorporation of cells in 3-dimensions directly in a HEWL hydrogel by using the ionic strength of cell culture media to drive gel formation while simultaneously incorporating cells homogeneously within the hydrogel. A schematic for this process is given in Figure 1. The resulting gel morphology and mechanical behavior have been explored using cryotransmission electron microscopy and oscillat...

show abstract

Designing Peptide‐Based Supramolecular Biomaterials

Jayawarna

Ulijn

2012

Supramolecular Chemistry

View full text Add to dashboard Cite

One rapidly emerging area where supramolecular chemistry can have a significant impact is in biomaterials science, and specifically in the design of cell‐contacting biomaterials. Aspects that are known to influence cell behavior at any particular time include chemical signals, mechanical properties (i.e., gel stiffness), and topographical signals related to fiber sizes and alignment. In this chapter, we provide an overview of current supramolecular chemistry strategies in the design of cell scaffolds based on peptides and their derivatives. The approaches discussed include those inspired by secondary or quaternary structures (α‐helix, β‐sheet, collagen triple helix) found in natural proteins as well as synthetic sequences such as aromatic and aliphatic peptide amphiphiles. We then discuss how supramolecular fibers based on peptides can be designed to control and direct (stem) cell behavior by engineering stiffness and chemical presentation of bioactive ligands.

show abstract

Self-assembly and gelation properties of α-helix versus β-sheet forming peptides

Cited by 141 publications

References 54 publications

Controlling network topology and mechanical properties of co‐assembling peptide hydrogels

Controlling network topology and mechanical properties of co‐assembling peptide hydrogels

Protein Fibrillar Hydrogels for three-Dimensional Tissue Engineering

Designing Peptide‐Based Supramolecular Biomaterials

Contact Info

Product

Resources

About